ArticleBiochemistry2007
Structure of the Na,K-ATPase regulatory protein FXYD1 in micelles.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 84 citations in OpenAlex.
- NaInternational journal of molecular sciences · 2024Review
- Discovery and Characterization of the Phospholemman/SIMP/Viroporin Superfamily.Microbial physiology · 2022Article
- MemDis: Predicting Disordered Regions in Transmembrane Proteins.International journal of molecular sciences · 2021Article
- Age-related changes in Na, K-ATPase expression, subunit isoform selection and assembly in the stria vascularis lateral wall of mouse cochlea.Hearing research · 2018Article
- Applications of NMR to membrane proteins.Archives of biochemistry and biophysics · 2017Review
- Optimal Bicelle Size q for Solution NMR Studies of the Protein Transmembrane Partition.Chemistry (Weinheim an der Bergstrasse, Germany) · 2017Article
- High quality NMR structures: a new force field with implicit water and membrane solvation for Xplor-NIH.Journal of biomolecular NMR · 2017Article
- Molecular Mechanisms and Kinetic Effects of FXYD1 and Phosphomimetic Mutants on Purified Human Na,K-ATPase.The Journal of biological chemistry · 2015Article
- Backbone structure of Yersinia pestis Ail determined in micelles by NMR-restrained simulated annealing with implicit membrane solvation.Journal of biomolecular NMR · 2015Article
- A Practical Implicit Membrane Potential for NMR Structure Calculations of Membrane Proteins.Biophysical journal · 2015Article
- Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation.Journal of biomolecular NMR · 2015Article
- Na+/Ca2+ exchange and Na+/K+-ATPase in the heart.The Journal of physiology · 2015Review
- Impact of phosphomimetic and non-phosphorylatable mutations of phospholemman on L-type calcium channels gating in HEK 293T cells.Journal of cellular and molecular medicine · 2015Article
- Structure of the Na,K-ATPase regulatory protein FXYD2b in micelles: implications for membrane-water interfacial arginines.Biochimica et biophysica acta · 2015Article
- Surface charges of the membrane crucially affect regulation of Na,K-ATPase by phospholemman (FXYD1).The Journal of membrane biology · 2013Article
- Protein structure validation and identification from unassigned residual dipolar coupling data using 2D-PDPA.Molecules (Basel, Switzerland) · 2013Article
- Na⁺/K⁺-ATPase E960 and phospholemman F28 are critical for their functional interaction.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments.Biochimica et biophysica acta · 2011Article
- The inhibitory effect of phospholemman on the sodium pump requires its palmitoylation.The Journal of biological chemistry · 2011Article
- Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
FXYD1 is a major regulatory subunit of the Na,K-ATPase and the principal substrate of hormone-regulated phosphorylation by c-AMP dependent protein kinases A and C in heart and skeletal muscle sarcolemma. It is a member of an evolutionarily conserved family of membrane proteins that regulate the function of the enzyme complex in a tissue-specific and physiological-state-specific manner. Here, we present the three-dimensional structure of FXYD1 determined in micelles by NMR spectroscopy. Structure determination was made possible by measuring residual dipolar couplings in weakly oriented micelle samples of the protein. This allowed us to obtain the relative orientations of the helical segments and information about the protein dynamics. The structural analysis was further facilitated by the inclusion of distance restraints, obtained from paramagnetic spin label relaxation enhancements, and by refinement with a micelle depth restraint, derived from paramagnetic Mn line broadening effects. The structure of FXYD1 provides the foundation for understanding its intra-membrane association with the Na,K-ATPase alpha subunit and suggests a mechanism whereby the phosphorylation of conserved Ser residues, by protein kinases A and C, could induce a conformational change in the cytoplasmic domain of the protein to modulate its interaction with the alpha subunit.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.